Leading Edge
Obituary
Howard Schachman (1918–2016)
Howard Schachman, renowned physical
chemist and protein chemist, professor
at the University of California, Berkeley,
extraordinary teacher, and a lifetime figh-
ter for civil liberties, died on August 5 in
Oakland California at age 97 from compli-
cations of pneumonia. Schachman’s
active career spanned fundamental work
on virus structure, the development of
the analytical ultracentrifuge and its use
to measure size and shape of proteins,
and incisive understanding on how en-
zymes control their activity. He remained
an active teacher until this year. In his life
he was deeply engaged in postwar
American science: its enthusiasm, its un-
imaginable triumphs, its prejudices, its
generosity, and its corruption. Schach-
man was kind and fair but a fighter when
it came to arrogance, dishonesty, and
injustice. He had an exceptional sense of
humor, and he found science a rich place
to practice his satirical art.
Howard Kapnek Schachman was born
in Philadelphia in 1918 less than a month
after the close of World War I. He re-
marked that he had no plans to be a scien-
tist and even thought about being a rabbi,
but in 1935 when he entered the Univer-
sity of Pennsylvania, he was
advised to go into engineering,
where jobs were available
even during the depression.
He transferred to MIT in chem-
ical engineering, but when he
graduated in 1939, he found
that for Jews there were virtu-
ally no opportunities in indus-
try. By chance he heard a
lecture about research on
tobacco mosaic virus under-
taken at the Rockefeller Insti-
tute, which then had a site
outside Princeton, N.J. He
applied for and was offered a
job as a technician. Benefiting
from good mentorship he
moved briefly to a PhD pro-
gram in physical chemistry at
Harvard, but within a year
Wendell Stanley, at Rockefel-
ler, asked Howard to come
back to his lab for a
wartime project on flu; Howard
managed to convince Princeton Univer-
sity to accept him as a part-time PhD
student with Walter Kauzmann. Soon
afterward, Howard married Ethel Lazarus,
his steady girlfriend from his undergradu-
ate days in Boston, whom he first met
when his MIT roommate invited Ethel out
for a date. In Princeton, Ethel was em-
ployed by the Emergency Committee of
Atomic Scientists and acted as a liaison
with Albert Einstein. Through this position,
she and Howard had a ringside seat at
extraordinarily consequential discussions
of science policy and government with
Oppenheimer, Bohr, and Einstein. Ho-
ward and Ethel (who died in 2013) were
together for almost 75 years; they were
lifetime partners on issues of politics and
social justice.
Stanley moved to Berkeley to set up
the Virus Lab and offered Howard an
instructorship. Howard began his new
job in 1948 by improving and exploiting
ultracentrifugation, which became the
most unambiguous method for charac-
terizing the size and shape of proteins
and the heterogeneity of DNA. His
biochemical, optical, and analytical inno-
vations were important for the develop-ment of protein chemistry and led to
many discoveries. One project, with
Pardee and Stanier, contributed to the
discovery of ribosomes. Soon after they
arrived, Berkeley was convulsed in con-
flict. The University had attached an in-
flammatory corollary to the state loyalty
oath, and Howard became one of the
leaders in opposing it and refusing to
sign it. He persisted until the very end
when a threat of firing and his concern
for his family caused him to sign under
strong protest; the 26 faculty who did
not sign were indeed dismissed. The fight
ultimately led to the State Supreme
Court, which concluded that the new
oath was unconstitutional.
After the ultracentrifuge period, Howard
was looking for a problem on protein func-
tion that would be worthy of all the power-
ful techniques now at his disposal. In
1962, he began a long and fruitful collab-
oration with John Gerhart, a newly minted
assistant professor who had discovered
feedback inhibition and cooperativity in
the enzyme aspartate transcarbamylase.
Gerhart’s inspired work had laid bare the
enzymatic properties of that molecule,
but had not probed its underlying struc-
tural and dynamical features.
This led to Howard’s 40 year
love affair with the enzyme.
Collaborating with Gerhart,
and then on his own, Howard
was able to measure the
concerted changes in the olig-
omeric protein, independently
from the local changes, by
sensitive sedimentation tech-
niques and spectral methods.
He reconstructed the molecule
in many different ways as hy-
brids of inactive and active
subunits and with specific mu-
tations and elegantly demon-
strated intra-allelic comple-
mentation. That large body of
work, bolstered by the X-ray
structure of the molecule
done by Bill Lipscomb at Har-
vard, gave science its most
intimate portrait of how allo-
steric regulation of enzymes
Howard Schachman. Photo courtesy of David Schachman. takes place.Cell 166 , September 8, 2016 1349